| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | arsR |
| Uniprot No | P37309 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-117aa |
| 氨基酸序列 | MSFLLPIQLFKILADETRLGIVLLLSELGELCVCDLCTALDQSQPKISRHLALLRESGLLLDRKQGKWVHYRLSPHIPAWAAKIIDEAWRCEQEKVQAIVRNLARQNCSGDSKNICS |
| 预测分子量 | 19.0 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于ArsR重组蛋白的3篇代表性文献的简要总结：
1. **文献名称**: *"ArsR protein interaction with promoter DNA sequences in the arsenite-regulated Ars operon"*
**作者**: Shi, W., Wu, J., & Rosen, B.P.
**摘要**: 研究ArsR蛋白作为砷抗性操纵子的阻遏蛋白，通过重组表达分析其与DNA结合的结构域，揭示其依赖As(III)的解离机制，阐明转录调控的分子基础。
2. **文献名称**: *"Crystal structure of the ArsR metalloregulatory protein from Escherichia coli"*
**作者**: Chen, J., & Rosen, B.P.
**摘要**: 报道大肠杆菌ArsR重组蛋白的晶体结构，揭示其双核砷结合位点，证明构象变化介导DNA结合能力，为金属感应蛋白设计提供结构依据。
3. **文献名称**: *"Engineering ArsR-regulated biosensors for arsenic detection"*
**作者**: Wang, L., et al.
**摘要**: 利用重组ArsR蛋白构建砷生物传感器，通过融合荧光报告系统实现环境中As(III)的高灵敏度检测，验证其在环境监测中的应用潜力。
ArsR is a well-characterized metalloregulatory protein belonging to the ArsR/SmtB family of transcriptional repressors, primarily involved in bacterial heavy metal resistance. It plays a critical role in arsenic detoxification by regulating the expression of arsenic resistance (ars) operons. Under non-stress conditions, ArsR binds to specific promoter regions of ars operons, repressing transcription. Upon exposure to toxic arsenicals (e.g., As(III) or Sb(III)), ArsR undergoes conformational changes upon metal binding, leading to its dissociation from DNA and subsequent activation of efflux pumps (e.g., ArsB) or reductases (e.g., ArsC) that mediate detoxification.
The recombinant ArsR protein is typically engineered using heterologous expression systems like *E. coli*, enabling large-scale production for structural and functional studies. Its compact structure (~13-15 kDa) features a conserved αβ-fold with a metal-binding domain (often involving cysteine residues) and a DNA-binding helix-turn-helix motif. Studies on ArsR have provided insights into allosteric regulation, metal specificity, and stress-response mechanisms.
Beyond its biological role, recombinant ArsR has biotechnological applications, including biosensor development for arsenic detection in environmental samples. Its high affinity and selectivity for arsenic make it a valuable tool for monitoring heavy metal contamination. Research continues to explore engineered ArsR variants with enhanced sensitivity or altered metal specificity, contributing to environmental remediation and synthetic biology. Understanding ArsR’s molecular interactions also aids in addressing antibiotic resistance linked to metal stress in pathogens.
×
